Associated Papers
Canonical and alternate mechanisms that regulate ubiquitylation by the E3 ligase parkin.
Basilone NT et al.
Biochemical Society Transactions, 2025
The Global Landscape of Genetic Variation in Parkinson's disease: Multi-Ancestry Insights into Established Disease Genes and their Translational Relevance.
Lange LM et al.
Medrxiv : the Preprint Server for Health Sciences, 2025
Capturing the catalytic intermediates of parkin ubiquitination.
Connelly EM et al.
Proceedings of the National Academy of Sciences of the United States of America, 2024
UBQLN2 and HSP70 participate in Parkin-mediated mitophagy by facilitating outer mitochondrial membrane rupture.
Ma Q et al.
Embo Reports, 2023
Comparative analysis of web-based programs for single amino acid substitutions in proteins.
Choudhury A et al.
Plos One, 2022
Multitasking guardian of mitochondrial quality: Parkin function and Parkinson's disease.
Kamienieva I et al.
Translational Neurodegeneration, 2021
The landscape of Parkin variants reveals pathogenic mechanisms and therapeutic targets in Parkinson's disease.
Yi W et al.
Human Molecular Genetics, 2019
Neuronal microtubules and proteins linked to Parkinson's disease: a relevant interaction?
Calogero AM et al.
Biological Chemistry, 2019
The M458L missense mutation disrupts the catalytic properties of Parkin.
Do YJ et al.
Febs Letters, 2018
A comprehensive computational study on pathogenic mis-sense mutations spanning the RING2 and REP domains of Parkin protein.
Biswas R et al.
Gene, 2017
Dual Function of Phosphoubiquitin in E3 Activation of Parkin.
Walinda E et al.
The Journal of Biological Chemistry, 2016
Covalent ISG15 conjugation positively regulates the ubiquitin E3 ligase activity of parkin.
Im E et al.
Open Biology, 2016
HydPred: a novel method for the identification of protein hydroxylation sites that reveals new insights into human inherited disease.
Li S et al.
Molecular Biosystems, 2016
Parkin maintains mitochondrial levels of the protective Parkinson's disease-related enzyme 17-β hydroxysteroid dehydrogenase type 10.
Bertolin G et al.
Cell Death and Differentiation, 2015
The TOMM machinery is a molecular switch in PINK1 and PARK2/PARKIN-dependent mitochondrial clearance.
Bertolin G et al.
Autophagy, 2013
Structure of the human Parkin ligase domain in an autoinhibited state.
Wauer T et al.
The Embo Journal, 2013
ER-stress-associated functional link between Parkin and DJ-1 via a transcriptional cascade involving the tumor suppressor p53 and the spliced X-box binding protein XBP-1.
Duplan E et al.
Journal of Cell Science, 2013
A molecular explanation for the recessive nature of parkin-linked Parkinson's disease.
Spratt DE et al.
Nature Communications, 2013
Parkin: much more than a simple ubiquitin ligase.
Alves da Costa C et al.
Neuro-degenerative Diseases, 2012
Genetic etiology of Parkinson disease associated with mutations in the SNCA, PARK2, PINK1, PARK7, and LRRK2 genes: a mutation update.
Nuytemans K et al.
Human Mutation, 2010
PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1.
Geisler S et al.
Nature Cell Biology, 2010
Transcriptional repression of p53 by parkin and impairment by mutations associated with autosomal recessive juvenile Parkinson's disease.
da Costa CA et al.
Nature Cell Biology, 2009
Parkin deficiency delays motor decline and disease manifestation in a mouse model of synucleinopathy.
Fournier M et al.
Plos One, 2009
Identification of a novel Zn2+-binding domain in the autosomal recessive juvenile Parkinson-related E3 ligase parkin.
Hristova VA et al.
The Journal of Biological Chemistry, 2009
Differential effects of Parkin and its mutants on protein aggregation, the ubiquitin-proteasome system, and neuronal cell death in human neuroblastoma cells.
Kyratzi E et al.
Journal of Neurochemistry, 2007
Parkin is an E3 ubiquitin-ligase for normal and mutant ataxin-2 and prevents ataxin-2-induced cell death.
Huynh DP et al.
Experimental Neurology, 2007
Familial-associated mutations differentially disrupt the solubility, localization, binding and ubiquitination properties of parkin.
Sriram SR et al.
Human Molecular Genetics, 2005
Parkin interacts with the proteasome subunit alpha4.
Dächsel JC et al.
Febs Letters, 2005
Novel parkin mutations detected in patients with early-onset Parkinson's disease.
Bertoli-Avella AM et al.
Movement Disorders : Official Journal of the Movement Disorder Society, 2005
Pathogenic mutations inactivate parkin by distinct mechanisms.
Henn IH et al.
Journal of Neurochemistry, 2005
Parkin counteracts symptoms in a Drosophila model of Parkinson's disease.
Haywood AF et al.
Bmc Neuroscience, 2004
The C289G and C418R missense mutations cause rapid sequestration of human Parkin into insoluble aggregates.
Gu WJ et al.
Neurobiology of Disease, 2003
The autosomal recessive juvenile Parkinson disease gene product, parkin, interacts with and ubiquitinates synaptotagmin XI.
Huynh DP et al.
Human Molecular Genetics, 2003
Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function.
Tsai YC et al.
The Journal of Biological Chemistry, 2003
Parkin prevents mitochondrial swelling and cytochrome c release in mitochondria-dependent cell death.
Darios F et al.
Human Molecular Genetics, 2003